Reviewed, UniProtKB/Swiss-Prot Q9Y2H9 (MAST1_HUMAN)

Names and origin

Protein names

Recommended name:
    Microtubule-associated serine/threonine-protein kinase 1
    EC=2.7.11.1
Alternative name(s):
    Syntrophin-associated serine/threonine-protein kinase

Gene names

Name:	MAST1
Synonyms:	KIAA0973

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Subunit structure	Part of a low affinity complex that associates with, but is distinct from, the post-synaptic density. Interacts with SNTB2 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic sideBy similarity. Cytoplasm › cytoskeletonBy similarity. Note= Colocalizes with syntrophins at the cell membrane By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 PDZ (DHR) domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAB51171.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cytoskeleton organization and biogenesis Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1570	1570	Microtubule-associated serine/threonine-protein kinase 1
Regions
	Domain	374 – 647	274	Protein kinase
	Domain	648 – 719	72	AGC-kinase C-terminal
	Domain	967 – 1055	89	PDZ
	Nucleotide binding	380 – 388	9	ATP By similarity
Sites
	Active site	497	1	Proton acceptor By similarity
	Binding site	403	1	ATP By similarity
Amino acid modifications
	Modified residue	161	1	Phosphoserine
	Modified residue	163	1	Phosphoserine
Natural variations
	Natural variant	269	1	A → T in a metastatic melanoma sample; somatic mutation.
	Natural variant	1240	1	H → Y in an ovarian serous carcinoma sample; somatic mutation.
	Natural variant	1292	1	P → S

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2H9-1 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: 189D24AE07B62A1E	FASTA	1,570	170,677
	10 20 30 40 50 60 MSDSLWTALS NFSMPSFPGG SMFRRTKSCR TSNRKSLILT STSPTLPRPH SPLPGHLGSS 70 80 90 100 110 120 PLDSPRNFSP NTPAHFSFAS SRRADGRRWS LASLPSSGYG TNTPSSTVSS SCSSQERLHQ 130 140 150 160 170 180 LPYQPTVDEL HFLSKHFGST ESITDEDGGR RSPAVRPRSR SLSPGRSPSS YDNEIVMMNH 190 200 210 220 230 240 VYKERFPKAT AQMEEKLRDF TRAYEPDSVL PLADGVLSFI HHQIIELARD CLTKSRDGLI 250 260 270 280 290 300 TTVYFYELQE NLEKLLQDAY ERSESLEVAF VTQLVKKLLI IISRPARLLE CLEFNPEEFY 310 320 330 340 350 360 HLLEAAEGHA KEGHLVKTDI PRYIIRQLGL TRDPFPDVVH LEEQDSGGSN TPEQDDLSEG 370 380 390 400 410 420 RSSKAKKPPG ENDFDTIKLI SNGAYGAVYL VRHRDTRQRF AMKKINKQNL ILRNQIQQAF 430 440 450 460 470 480 VERDILTFAE NPFVVGMFCS FETRRHLCMV MEYVEGGDCA TLLKNIGALP VEMARMYFAE 490 500 510 520 530 540 TVLALEYLHN YGIVHRDLKP DNLLITSMGH IKLTDFGLSK MGLMSLTTNL YEGHIEKDAR 550 560 570 580 590 600 EFLDKQVCGT PEYIAPEVIL RQGYGKPVDW WAMGIILYEF LVGCVPFFGD TPEELFGQVI 610 620 630 640 650 660 SDDILWPEGD EALPTEAQLL ISSLLQTNPL VRLGAGGAFE VKQHSFFRDL DWTGLLRQKA 670 680 690 700 710 720 EFIPHLESED DTSYFDTRSD RYHHVNSYDE DDTTEEEPVE IRQFSSCSPR FSKVYSSMEQ 730 740 750 760 770 780 LSQHEPKTPV AAAGSSKREP STKGPEEKVA GKREGLGGLT LREKTWRGGS PEIKRFSASE 790 800 810 820 830 840 ASFLEGEASP PLGARRRFSA LLEPSRFSAP QEDEDEARLR RPPRPSSDPA GSLDARAPKE 850 860 870 880 890 900 ETQGEGTSSA GDSEATDRPR PGDLCPPSKD GDASGPRATN DLVLRRARHQ QMSGDVAVEK 910 920 930 940 950 960 RPSRTGGKVI KSASATALSV MIPAVDPHGS SPLASPMSPR SLSSNPSSRD SSPSRDYSPA 970 980 990 1000 1010 1020 VSGLRSPITI QRSGKKYGFT LRAIRVYMGD TDVYSVHHIV WHVEEGGPAQ EAGLCAGDLI 1030 1040 1050 1060 1070 1080 THVNGEPVHG MVHPEVVELI LKSGNKVAVT TTPFENTSIR IGPARRSSYK AKMARRNKRP 1090 1100 1110 1120 1130 1140 SAKEGQESKK RSSLFRKITK QSNLLHTSRS LSSLNRSLSS SDSLPGSPTH GLPARSPTHS 1150 1160 1170 1180 1190 1200 YRSTPDSAYL GASSQSSSPA SSTPNSPASS ASHHIRPSTL HGLSPKLHRQ YRSARCKSAG 1210 1220 1230 1240 1250 1260 NIPLSPLAHT PSPTQASPPP LPGHTVGSSH TTQSFPAKLH SSPPVVRPRP KSAEPPRSPL 1270 1280 1290 1300 1310 1320 LKRVQSAEKL GASLSADKKG ALRKHSLEVG HPDFRKDFHG ELALHSLAES DGETPPVEGL 1330 1340 1350 1360 1370 1380 GAPRQVAVRR LGRQESPLSL GADPLLPEGA SRPPVSSKEK ESPGGAEACT PPRATTPGGR 1390 1400 1410 1420 1430 1440 TLERDVGCTR HQSVQTEDGT GGMARAVAKA ALSPVQEHET GRRSSSGEAG TPLVPIVVEP 1450 1460 1470 1480 1490 1500 ARPGAKAVVP QPLGADSKGL QEPAPLAPSV PEAPRGRERW VLEVVEERTT LSGPRSKPAS 1510 1520 1530 1540 1550 1560 PKLSPEPQTP SLAPAKCSAP SSAVTPVPPA SLLGSGTKPQ VGLTSRCPAE AVPPAGLTKK 1570 GVSSPAPPGP

References

[1]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed: 10231032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-1570. Tissue: Brain.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-163, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-269; TYR-1240 AND SER-1292.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB023190 mRNA. Translation: BAA76817.1. Different initiation. AC020934 Genomic DNA. No translation available. AD000092 Genomic DNA. Translation: AAB51171.1. Sequence problems. BC027985 mRNA. Translation: AAH27985.1. Different initiation.
PIR	T45070.
RefSeq	NP_055790.1.
UniGene	Hs.227489
3D structure databases
HSSP	HSSP built from PDB template 1MRY based on UniProtKB P31751.
ModBase	Search...
PTM databases
PhosphoSite	Q9Y2H9.
Proteomic databases
PeptideAtlas	Q9Y2H9.
Genome annotation databases
Ensembl	ENSG00000105613. Homo sapiens. [Contig view]
GeneID	22983.
KEGG	hsa:22983.
Organism-specific databases
H-InvDB	HIX0014808.
HGNC	HGNC:19034. MAST1.
PharmGKB	PA134946727.
HUGE	Search...
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q9Y2H9.
HOVERGEN	Q9Y2H9.
Gene expression databases
CleanEx	HS_MAST1.
GermOnline	ENSG00000105613. Homo sapiens.
Family and domain databases
InterPro	IPR015022. DUF1908. IPR001478. PDZ. IPR000961. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF08926. DUF1908. 1 hit. PF00595. PDZ. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00228. PDZ. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50106. PDZ. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

MAST1_HUMAN

Accession

Primary (citable) accession number: Q9Y2H9
Secondary accession number(s): O00114, Q8N6X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	July 22, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)